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PNO_EUGGR
ID   PNO_EUGGR               Reviewed;        1803 AA.
AC   Q94IN5; Q9FZP8;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Pyruvate dehydrogenase [NADP(+)], mitochondrial;
DE            EC=1.2.1.51 {ECO:0000269|PubMed:3110154};
DE   AltName: Full=Aquacobalamin reductase [NADPH];
DE   AltName: Full=EgPNOmt;
DE   AltName: Full=Pyruvate:NADP(+) oxidoreductase;
DE   Flags: Precursor;
GN   Name=PNO;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039 {ECO:0000312|EMBL:CAC37628.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11023353; DOI=10.1016/s0014-5793(00)01882-2;
RA   Nakazawa M., Inui H., Yamaji R., Yamamoto T., Takenaka S., Ueda M.,
RA   Nakano Y., Miyatake K.;
RT   "The origin of pyruvate:NADP+ oxidoreductase in mitochondria of Euglena
RT   gracilis.";
RL   FEBS Lett. 479:155-156(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=SAG1224-5/25;
RX   PubMed=11319255; DOI=10.1093/oxfordjournals.molbev.a003853;
RA   Rotte C., Stejskal F., Zhu G., Keithly J.S., Martin W.;
RT   "Pyruvate: NADP oxidoreductase from the mitochondrion of Euglena gracilis
RT   and from the apicomplexan Cryptosporidium parvum: a biochemical relic
RT   linking pyruvate metabolism in mitochondriate and amitochondriate
RT   protists.";
RL   Mol. Biol. Evol. 18:710-720(2001).
RN   [3]
RP   PROTEIN SEQUENCE OF 38-53 AND 1240-1259.
RX   PubMed=1910287; DOI=10.1016/0003-9861(91)90040-p;
RA   Inui H., Yamaji R., Saidoh H., Miyatake K., Nakano Y., Kitaoka S.;
RT   "Pyruvate:NADP+ oxidoreductase from Euglena gracilis: limited proteolysis
RT   of the enzyme with trypsin.";
RL   Arch. Biochem. Biophys. 286:270-276(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 1240-1255, FUNCTION, AND CHARACTERIZATION.
RX   PubMed=8373179; DOI=10.1006/abbi.1993.1441;
RA   Watanabe F., Yamaji R., Isegawa Y., Yamamoto T., Tamura Y., Nakano Y.;
RT   "Characterization of aquacobalamin reductase (NADPH) from Euglena
RT   gracilis.";
RL   Arch. Biochem. Biophys. 305:421-427(1993).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX   PubMed=3110154; DOI=10.1016/s0021-9258(18)48057-x;
RA   Inui H., Ono K., Miyatake K., Nakano Y., Kitaoka S.;
RT   "Purification and characterization of pyruvate:NADP+ oxidoreductase in
RT   Euglena gracilis.";
RL   J. Biol. Chem. 262:9130-9135(1987).
RN   [6]
RP   FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=12623066; DOI=10.1016/s0003-9861(02)00749-x;
RA   Nakazawa M., Takenaka S., Ueda M., Inui H., Nakano Y., Miyatake K.;
RT   "Pyruvate:NADP(+) oxidoreductase is stabilized by its cofactor, thiamin
RT   pyrophosphate, in mitochondria of Euglena gracilis.";
RL   Arch. Biochem. Biophys. 411:183-188(2003).
CC   -!- FUNCTION: Pyruvate dehydrogenase [NADP(+)] is one of three enzymes
CC       participating in respiratory metabolism. The enzyme is also active with
CC       2-oxobutyrate and oxaloacetate. The enzyme is oxygen sensitive.
CC       {ECO:0000269|PubMed:12623066, ECO:0000269|PubMed:3110154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + NADP(+) + pyruvate = acetyl-CoA + CO2 + NADPH;
CC         Xref=Rhea:RHEA:17425, ChEBI:CHEBI:15361, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.51;
CC         Evidence={ECO:0000269|PubMed:3110154};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:12623066};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:12623066};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:12623066};
CC       Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:12623066};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:12623066};
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000269|PubMed:3110154};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=210 uM for pyruvate {ECO:0000269|PubMed:3110154};
CC         KM=8 uM for CoA {ECO:0000269|PubMed:3110154};
CC         KM=30 uM for NADP(+) {ECO:0000269|PubMed:3110154};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:3110154};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:3110154};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12623066,
CC       ECO:0000269|PubMed:3110154}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11319255,
CC       ECO:0000269|PubMed:12623066}.
CC   -!- INDUCTION: Expressed in both aerobic and anaerobic conditions.
CC   -!- MISCELLANEOUS: Arose from gene fusion of pyruvate:ferredoxin
CC       oxidoreductase and cytochrome-P450 reductase. Gene fusion has only been
CC       found in Euglena and Cryptosporidium. {ECO:0000303|PubMed:11023353,
CC       ECO:0000303|PubMed:11319255}.
CC   -!- MISCELLANEOUS: Euglena cells absolutely require thiamine for growth due
CC       to the lack of a pyrimidine formation biosynthetic pathway. Thiamine is
CC       actively taken up into the cells and is used as a cofactor after being
CC       converted to TPP (thiamine pyrophosphate).
CC       {ECO:0000269|PubMed:12623066}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       pyruvate:ferredoxin/flavodoxin oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AB021127; BAB12024.1; -; mRNA.
DR   EMBL; AJ278425; CAC37628.1; -; mRNA.
DR   PIR; S36876; S36876.
DR   AlphaFoldDB; Q94IN5; -.
DR   SMR; Q94IN5; -.
DR   PRIDE; Q94IN5; -.
DR   KEGG; ag:BAB12024; -.
DR   BioCyc; MetaCyc:MON-17049; -.
DR   BRENDA; 1.2.1.51; 2197.
DR   SABIO-RK; Q94IN5; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0050243; F:pyruvate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IDA:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IDA:UniProtKB.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.920.10; -; 1.
DR   Gene3D; 4.10.780.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM00890; EKR; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   TIGRFAMs; TIGR02176; pyruv_ox_red; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; FAD; Flavoprotein;
KW   FMN; Iron; Iron-sulfur; Metal-binding; Mitochondrion; NADP; Oxidoreductase;
KW   Repeat; Thiamine pyrophosphate; Transit peptide; Transport.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1910287"
FT   CHAIN           38..1803
FT                   /note="Pyruvate dehydrogenase [NADP(+)], mitochondrial"
FT                   /id="PRO_0000023867"
FT   DOMAIN          747..776
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          802..831
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          1248..1391
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          1425..1650
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         756
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         759
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         762
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         766
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         811
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         814
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         817
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         821
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         1458..1469
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         1585..1595
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        50
FT                   /note="P -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="H -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="V -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        598..599
FT                   /note="NV -> KL (in Ref. 1; BAB12024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1256
FT                   /note="T -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1558
FT                   /note="M -> T (in Ref. 1; BAB12024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1673..1674
FT                   /note="ER -> DG (in Ref. 1; BAB12024)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1803 AA;  199821 MW;  5AFB6E3869CADCC6 CRC64;
     MKQSVRPIIS NVLRKEVALY STIIGQDKGK EPTGRTYTSG PKPASHIEVP HHVTVPATDR
     TPNPDAQFFQ SVDGSQATSH VAYALSDTAF IYPITPSSVM GELADVWMAQ GRKNAFGQVV
     DVREMQSEAG AAGALHGALA AGAIATTFTA SQGLLLMIPN MYKIAGELMP SVIHVAAREL
     AGHALSIFGG HADVMAVRQT GWAMLCSHTV QQSHDMALIS HVATLKSSIP FVHFFDGFRT
     SHEVNKIKML PYAELKKLVP PGTMEQHWAR SLNPMHPTIR GTNQSADIYF QNMESANQYY
     TDLAEVVQET MDEVAPYIGR HYKIFEYVGA PDAEEVTVLM GSGATTVNEA VDLLVKRGKK
     VGAVLVHLYR PWSTKAFEKV LPKTVKRIAA LDRCKEVTAL GEPLYLDVSA TLNLFPERQN
     VKVIGGRYGL GSKDFIPEHA LAIYANLASE NPIQRFTVGI TDDVTGTSVP FVNERVDTLP
     EGTRQCVFWG IGSDGTVGAN RSAVRIIGDN SDLMVQAYFQ FDAFKSGGVT SSHLRFGPKP
     ITAQYLVTNA DYIACHFQEY VKRFDMLDAI REGGTFVLNS RWTTEDMEKE IPADFRRNVA
     QKKVRFYNVD ARKICDSFGL GKRINMLMQA CFFKLSGVLP LAEAQRLLNE SIVHEYGKKG
     GKVVEMNQAV VNAVFAGDLP QEVQVPAAWA NAVDTSTRTP TGIEFVDKIM RPLMDFKGDQ
     LPVSVMTPGG TFPVGTTQYA KRAIAAFIPQ WIPANCTQCN YCSYVCPHAT IRPFVLTDQE
     VQLAPESFVT RKAKGDYQGM NFRIQVAPED CTGCQVCVET CPDDALEMTD AFTATPVQRT
     NWEFAIKVPN RGTMTDRYSL KGSQFQQPLL EFSGACEGCG ETPYVKLLTQ LFGERTVIAN
     ATGCSSIWGG TAGLAPYTTN AKGQGPAWGN SLFEDNAEFG FGIAVANAQK RSRVRDCILQ
     AVEKKVADEG LTTLLAQWLQ DWNTGDKTLK YQDQIIAGLA QQRSKDPLLE QIYGMKDMLP
     NISQWIIGGD GWANDIGFGG LDHVLASGQN LNVLVLDTEM YSNTGGQASK STHMASVAKF
     ALGGKRTNKK NLTEMAMSYG NVYVATVSHG NMAQCVKAFV EAESYDGPSL IVGYAPCIEH
     GLRAGMARMV QESEAAIATG YWPLYRFDPR LATEGKNPFQ LDSKRIKGNL QEYLDRQNRY
     VNLKKNNPKG ADLLKSQMAD NITARFNRYR RMLEGPNTKA AAPSGNHVTI LYGSETGNSE
     GLAKELATDF ERREYSVAVQ ALDDIDVADL ENMGFVVIAV STCGQGQFPR NSQLFWRELQ
     RDKPEGWLKN LKYTVFGLGD STYYFYCHTA KQIDARLAAL GAQRVVPIGF GDDGDEDMFH
     TGFNNWIPSV WNELKTKTPE EALFTPSIAV QLTPNATPQD FHFAKSTPVL SITGAERITP
     ADHTRNFVTI RWKTDLSYQV GDSLGVFPEN TRSVVEEFLQ YYGLNPKDVI TIENKGSREL
     PHCMAVGDLF TKVLDILGKP NNRFYKTLSY FAVDKAEKER LLKIAEMGPE YSNILSEMYH
     YADIFHMFPS ARPTLQYLIE MIPNIKPRYY SISSAPIHTP GEVHSLVLID TWITLSGKHR
     TGLTCTMLEH LQAGQVVDGC IHPTAMEFPD HEKPVVMCAM GSGLAPFVAF LRERSTLRKQ
     GKKTGNMALY FGNRYEKTEF LMKEELKGHI NDGLLTLRCA FSRDDPKKKV YVQDLIKMDE
     KMMYDYLVVQ KGSMYCCGSR SFIKPVQESL KHCFMKAGGL TAEQAENEVI DMFTTGRYNI
     EAW
 
 
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